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Angiotensin I
Angiotensin is a peptide hormone that causes vasoconstriction and an increase in blood pressure. It is part of the renin–angiotensin system, which regulates blood pressure. Angiotensin also stimulates the release of aldosterone from the adrenal cortex to promote sodium retention by the kidneys. An oligopeptide, angiotensin is a hormone and a dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. Angiotensin was isolated in the late 1930s (first named "angiotonin" or "hypertensin", later renamed "angiotensin" as a consensus by the 2 groups that independently discovered it) and subsequently characterized and synthesized by groups at the Cleveland Clinic and Ciba laboratories. Precursor and types Angiotensinogen Angiotensinogen is an α-2-globulin synthesized in the liver and is a precursor for angiotensin, but has also been indicated as having many other roles not related to angiotensin peptides. It is a member of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide Hormone
Peptide hormones are hormones composed of peptide molecules. These hormones influence the endocrine system of animals, including humans. Most hormones are classified as either amino-acid-based hormones (amines, peptides, or proteins) or steroid hormones. Amino-acid-based hormones are water-soluble and act on target cells via second messenger systems, whereas steroid hormones, being lipid-soluble, diffuse through plasma membranes to interact directly with intracellular receptors in the cell nucleus. Like all peptides, peptide hormones are synthesized in cell (biology), cells from amino acids based on Messenger RNA, mRNA transcripts, which are derived from DNA templates inside the cell nucleus. The initial precursors, known as preprohormones, undergo processing in the endoplasmic reticulum. This includes the removal of the N-terminal signal peptide and, in some cases, glycosylation, yielding prohormones. These prohormones are then packaged into secretory vesicle (biology), vesicles, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Renin
Renin ( etymology and pronunciation), also known as an angiotensinogenase, is an aspartic protease protein and enzyme secreted by the kidneys that participates in the body's renin-angiotensin-aldosterone system (RAAS)—also known as the renin-angiotensin-aldosterone axis—that increases the volume of extracellular fluid (blood plasma, lymph, and interstitial fluid) and causes arterial vasoconstriction. Thus, it increases the body's mean arterial blood pressure. Renin is not commonly referred to as a hormone, although it has a receptor, the (pro)renin receptor, also known as the renin receptor and prorenin receptor (see also below), as well as enzymatic activity with which it hydrolyzes angiotensinogen to angiotensin I. Biochemistry and physiology Structure The primary structure of renin precursor consists of 406 amino acids with a pre- and a pro-segment carrying 20 and 46 amino acids, respectively. Mature renin contains 340 amino acids and has a mass of 37 kDa. Secr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Macula Densa
In the kidney, the macula densa is an area of closely packed specialized cells lining the wall of the distal tubule where it touches the glomerulus. Specifically, the macula densa is found in the terminal portion of the distal straight tubule ( thick ascending limb of the loop of Henle), after which the distal convoluted tubule begins. The cells of the macula densa are sensitive to the concentration of sodium chloride in the thick ascending loop of henle. A decrease in sodium chloride concentration initiates a signal from the macula densa that has two effects: (1) it decreases resistance to blood flow in the afferent arterioles, which raises glomerular hydrostatic pressure and helps return the glomerular filtration rate (GFR) toward normal, and (2) it increases renin release from the juxtaglomerular cells of the afferent and efferent arterioles, which are the major storage sites for renin. As such, an increase in sodium chloride concentration would result in vasoconstrictio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Juxtaglomerular Cell
Juxtaglomerular cells (JG cells), also known as juxtaglomerular granular cells are cells in the kidney that synthesize, store, and secrete the enzyme renin. They are specialized smooth muscle cells mainly in the walls of the afferent arterioles (and some in the efferent arterioles) that deliver blood to the glomerulus. They are located near the glomerulus, hence the name. In synthesizing renin, they play a critical role in the renin–angiotensin system and thus in autoregulation of the kidney. Juxtaglomerular cells secrete renin in response to a drop in pressure detected by stretch receptors in the vascular walls, or when stimulated by macula densa cells. Macula densa cells are located in the distal convoluted tubule, and stimulate juxtaglomerular cells to release renin when they detect a drop in chloride concentration in tubular fluid. Together, juxtaglomerular cells, extraglomerular mesangial cells and macula densa cells comprise the juxtaglomerular apparatus. In a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kidney
In humans, the kidneys are two reddish-brown bean-shaped blood-filtering organ (anatomy), organs that are a multilobar, multipapillary form of mammalian kidneys, usually without signs of external lobulation. They are located on the left and right in the retroperitoneal space, and in adult humans are about in length. They receive blood from the paired renal artery, renal arteries; blood exits into the paired renal veins. Each kidney is attached to a ureter, a tube that carries excreted urine to the urinary bladder, bladder. The kidney participates in the control of the volume of various body fluids, fluid osmolality, Acid-base homeostasis, acid-base balance, various electrolyte concentrations, and removal of toxins. Filtration occurs in the glomerulus (kidney), glomerulus: one-fifth of the blood volume that enters the kidneys is filtered. Examples of substances reabsorbed are solute-free water, sodium, bicarbonate, glucose, and amino acids. Examples of substances secreted are hy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (carboxyl g ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Valine
Valine (symbol Val or V) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated −NH3+ form under biological conditions), an α- carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid. Valine is essential in humans, meaning the body cannot synthesize it; it must be obtained from dietary sources which are foods that contain proteins, such as meats, dairy products, soy products, beans and legumes. It is encoded by all codons starting with GU (GUU, GUC, GUA, and GUG). History and etymology Valine was first isolated from casein in 1901 by Hermann Emil Fischer. The name valine comes from its structural similarity to valeric acid, which in turn is named after the plant valerian due to the presence of the acid in the roots of the plant. Nomenclature According to IUPAC, carbon atoms forming v ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Leucine
Leucine (symbol Leu or L) is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α-Carboxylic acid, carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain Isobutyl, isobutyl group, making it a Chemical polarity, non-polar Aliphatic compound, aliphatic amino acid. It is Essential amino acid, essential in humans, meaning the body cannot synthesize it; it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is genetic code, encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG. Leucine is named after the Greek language, Greek word for "white": ''λευκός'' (''leukós'', "white"), after its common appearance as a white powder, a property it shares with many ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide Bond
In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein chain. It can also be called a eupeptide bond to distinguish it from an isopeptide bond, which is another type of amide bond between two amino acids. Synthesis When two amino acids form a '' dipeptide'' through a ''peptide bond'', it is a type of condensation reaction. In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other. One loses a hydrogen and oxygen from its carboxyl group (COOH) and the other loses a hydrogen from its amino group (NH2). This reaction produces a molecule of water (H2O) and two amino acids joined by a peptide bond (−CO−NH−). The two joined amino acids are called a dipeptide. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Angiotensinogen
Angiotensin is a peptide hormone that causes vasoconstriction and an increase in blood pressure. It is part of the renin–angiotensin system, which regulates blood pressure. Angiotensin also stimulates the release of aldosterone from the adrenal cortex to promote sodium retention by the kidneys. An oligopeptide, angiotensin is a hormone and a dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. Angiotensin was isolated in the late 1930s (first named "angiotonin" or "hypertensin", later renamed "angiotensin" as a consensus by the 2 groups that independently discovered it) and subsequently characterized and synthesized by groups at the Cleveland Clinic and Ciba laboratories. Precursor and types Angiotensinogen Angiotensinogen is an α-2-globulin synthesized in the liver and is a precursor for angiotensin, but has also been indicated as having many other roles not related to angiotensin peptides. It is a member ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
